NCBS Home page
Accession List
Pathway List
Search
Authorized Users
Help
News archives

Accession Type:
Network
Osc_Ca_
IP3metabolism
MIPP
CaMKII
 Molecule
 Enzyme
 Reaction
CaM
PKC
IP3-3K
Gq
PLCbeta
134_dephos
145_dephos
IP4-system
IHP-system
1345_dephos
CaRegulation
Othmer-Tang-mode
l

Enter a Search String

Special character and space not allowed in the query term. Search string should be at least 2 characters long.
Search in: Search for Match By

Enzyme List for pathway CaMKII (Pathway Number 159)

 Molecule Name/
Site Name
Km (uM) kcat (1/s)Ratio
(k2/k3)
Enzyme TypeSubstrate Product
1 Enzyme Activity:
auton_286

Enzyme Molecule:
tot_autonomous_
CaMKII
0.000004166670.54explicit E-S complexCaMKII-CaM
  • CaMKII-thr286*-C
    aM

  •   The autonomous rate has a slightly higher Km than the CaM-bound rate, but Vmax is the same. Hanson and Schulman 1992 Ann Rev Biochem 61:559-601 and Hanson and Schulman 1992 JBC 267(24):17216-17224
    2 Enzyme Activity:
    auton_305

    Enzyme Molecule:
    tot_autonomous_
    CaMKII
    0.0000041666764explicit E-S complexCaMKII-thr286
    CaMKII***
      See Hanson and Schulman 1992 JBC 267(24):17216-17224 for afterburst rates of phosphorylation
    3 Enzyme Activity:
    CaM-CaMK-phos

    Enzyme Molecule:
    tot_CaM_CaMKII
    1.600010.54explicit E-S complexIP3_3K
    IP3_3K*
      rates referred from standard CaM-CaMKII phosphorylation rates
    4 Enzyme Activity:
    CaM-CaMK-phos1

    Enzyme Molecule:
    tot_CaM_CaMKII
    1.599980.54explicit E-S complexIP3_3K_CaM
    IP3_3K_CaM*
      rates referred from standard CaM-CaMKII phosphorylation rates
    5 Enzyme Activity:
    CaMK-phos

    Enzyme Molecule:
    tot_autonomous_
    CaMKII
    2.499990.54explicit E-S complexIP3_3K
    IP3_3K*
      rates referred from standard CaMKII phosphorylation rates
    6 Enzyme Activity:
    CaMK-phos1

    Enzyme Molecule:
    tot_autonomous_
    CaMKII
    2.499950.54explicit E-S complexIP3_3K_CaM
    IP3_3K_CaM*
      rates referred from standard CaMKII phosphorylation rates
    7 Enzyme Activity:
    CaM_act_286

    Enzyme Molecule:
    tot_CaM_CaMKII
    0.000002705630.54explicit E-S complexCaMKII-CaM
  • CaMKII-thr286*-C
    aM

  •   See Hanson and Schulman 1992 JBC 267(24):17216-17224
    8 Enzyme Activity:
    CaM_act_305

    Enzyme Molecule:
    tot_CaM_CaMKII
    0.0000027056364explicit E-S complexCaMKII-thr286
    CaMKII***
      Rates from autocamtide phosphorylation, from Hanson and Schulman JBC 267:24 17216-17224 1992. See especially Fig 5.
    9 Enzyme Activity:
    Deph-thr286

    Enzyme Molecule:
    PP1-active
    5.099070.354explicit E-S complex
  • CaMKII-thr286*-C
    aM

  • CaMKII-CaM
      The rates are from Stralfors et al Eur J Biochem 149 295-303 giving Vmax = 5.7 umol/min giving k3 = 3.5/sec and k2 = 14. Foulkes et al Eur J Biochem 132 309-313 1983 give Km = 5.1 uM so k1 becomes 5.72e-6 Simonelli 1984 (Grad Thesis, CUNY) showed that other substrates are about 1/10 rate of phosphorylase a, so we reduce k1,k2,k3 by 10 to 5.72e-7, 1.4, 0.35. This gives the final Km of 5.1, and Vmax of 0.35/sec.
    10 Enzyme Activity:
    Deph-thr286c

    Enzyme Molecule:
    PP1-active
    5.099070.354explicit E-S complexCaMKII***
    CaMK-thr306
      Dephosphorylation tempkin are assumed to be the same for all phosphorylation sites on CaMKII. The rates are from Stralfors et al Eur J Biochem 149 295-303 giving Vmax = 5.7 umol/min giving k3 = 3.5/sec and k2 = 14. Foulkes et al Eur J Biochem 132 309-313 1983 give Km = 5.1 uM so k1 becomes 5.72e-6 Simonelli 1984 (Grad Thesis, CUNY) showed that other substrates are about 1/10 rate of phosphorylase a, so we reduce k1,k2,k3 by 10 to 5.72e-7, 1.4, 0.35. This gives the final Km of 5.1, and Vmax of 0.35/sec.
    11 Enzyme Activity:
    Deph-thr305

    Enzyme Molecule:
    PP1-active
    5.099070.354explicit E-S complexCaMKII***
    CaMKII-thr286
      Dephosphorylation tempkin are assumed to be the same for all phosphorylation sites on CaMKII. The rates are from Stralfors et al Eur J Biochem 149 295-303 giving Vmax = 5.7 umol/min giving k3 = 3.5/sec and k2 = 14. Foulkes et al Eur J Biochem 132 309-313 1983 give Km = 5.1 uM so k1 becomes 5.72e-6 Simonelli 1984 (Grad Thesis, CUNY) showed that other substrates are about 1/10 rate of phosphorylase a, so we reduce k1,k2,k3 by 10 to 5.72e-7, 1.4, 0.35. This gives the final Km of 5.1, and Vmax of 0.35/sec.
    12 Enzyme Activity:
    Deph-thr306

    Enzyme Molecule:
    PP1-active
    5.099070.354explicit E-S complexCaMK-thr306
    CaMKII
      Dephosphorylation tempkin are assumed to be the same for all phosphorylation sites on CaMKII. The rates are from Stralfors et al Eur J Biochem 149 295-303 giving Vmax = 5.7 umol/min giving k3 = 3.5/sec and k2 = 14. Foulkes et al Eur J Biochem 132 309-313 1983 give Km = 5.1 uM so k1 becomes 5.72e-6 Simonelli 1984 (Grad Thesis, CUNY) showed that other substrates are about 1/10 rate of phosphorylase a, so we reduce k1,k2,k3 by 10 to 5.72e-7, 1.4, 0.35. This gives the final Km of 5.1, and Vmax of 0.35/sec.
    13 Enzyme Activity:
    Deph_thr286b

    Enzyme Molecule:
    PP1-active
    5.099070.354explicit E-S complexCaMKII-thr286
    CaMKII
      Rates are assumed to be the same for all phosphorylation sites on CaMKII. The rates are from Stralfors et al Eur J Biochem 149 295-303 giving Vmax = 5.7 umol/min giving k3 = 3.5/sec and k2 = 14. Foulkes et al Eur J Biochem 132 309-313 1983 give Km = 5.1 uM so k1 becomes 5.72e-6 Simonelli 1984 (Grad Thesis, CUNY) showed that other substrates are about 1/10 rate of phosphorylase a, so we reduce k1,k2,k3 by 10 to 5.72e-7, 1.4, 0.35. This gives the final Km of 5.1, and Vmax of 0.35/sec.


    Pathway Details   Molecule List  Enzyme List   Reaction List  


    Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
    This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details.